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Database: UniProt
Entry: E4KNH5_9LACT
LinkDB: E4KNH5_9LACT
Original site: E4KNH5_9LACT 
ID   E4KNH5_9LACT            Unreviewed;       544 AA.
AC   E4KNH5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=HMPREF9257_0337 {ECO:0000313|EMBL:EFR31511.1};
OS   Eremococcus coleocola ACS-139-V-Col8.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX   NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR31511.1, ECO:0000313|Proteomes:UP000005990};
RN   [1] {ECO:0000313|EMBL:EFR31511.1, ECO:0000313|Proteomes:UP000005990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR31511.1,
RC   ECO:0000313|Proteomes:UP000005990};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938,
CC         ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFR31511.1}.
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DR   EMBL; AENN01000011; EFR31511.1; -; Genomic_DNA.
DR   RefSeq; WP_006418045.1; NZ_AENN01000011.1.
DR   AlphaFoldDB; E4KNH5; -.
DR   STRING; 908337.HMPREF9257_0337; -.
DR   eggNOG; COG0508; Bacteria.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000005990; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005990};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:EFR31511.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          115..190
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          236..273
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          197..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  57723 MW;  B93392C4F5026CFB CRC64;
     MAFKFTLPEL GEGIHEGEIV SILVSEGQAI SEDDIILEVQ NDKAVEELPT PVTGTVKSIK
     VSEGDVVTVG DVLIEIDAEG YEGEDLPEEP AVTAAAEEDL LATKAADQPG QASGYFNFTL
     PELGEGIHEG EIVSWLVSED DTVAEDDIIL EVQNDKAVEE LPTPYAGKIV KIHAQPGQVV
     QVGDILVEID APDFEGDGSS AAPAVSDSAS AAPAAAASQP GQVSGRAGTS PAGHVLAMPS
     VRKLARDKGI DINLVVPTGK GGRVTEADVN NFNPNQTASA PAEKTAPATA GAATEKTAPA
     KKATPLVSNA ERTTREKMSG TRKAIAKAMT NSKHTSPHVT HFDEIEVSKL WDHRKKFKGI
     AAERDTKLTF LPYAVKALVA ALKKYPILNA SLDDATNEIV YHNYYNIGIA TDTDHGLYVP
     NIKDANAKSM FDIADEITEL ANKAHDSKLS AGEMRDGTIT ISNIGSAGGK WFTPIINHPE
     VAILGFGSIV QQPIVDENGE LAVGRMIKLS LSYDHRVIDG ATAQKAMNEI KRYLADPELL
     LMEG
//
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